Characterization, Kinetic, and Thermodynamic Studies of Marine Pectinase From<i>Bacillus subtilis</i>

Joshi, Manasi; Nerurkar, Madhura; Adivarekar, Ravindra V.

doi:10.1080/10826068.2014.907181

Cited by 17 publications

(10 citation statements)

References 42 publications

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“…In addition, the differences inΔG # across the temperature range were about 6.5 and 7.1% for Lipase PS and Palatase, respectively ( Table 4 ). Similar observations were found with several heat-stable structures [ 61 , 62 ] which may indicate a decrease in the enzyme lability to unfold as the temperature increased.…”

Section: Resultssupporting

confidence: 87%

Kinetic Modeling, Thermodynamic Approach and Molecular Dynamics Simulation of Thermal Inactivation of Lipases from Burkholderia cepacia and Rhizomucor miehei

Ortega

Sáez

Palacios

et al. 2022

IJMS

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The behavior against temperature and thermal stability of enzymes is a topic of importance for industrial biocatalysis. This study focuses on the kinetics and thermodynamics of the thermal inactivation of Lipase PS from B. cepacia and Palatase from R. miehei. Thermal inactivation was investigated using eight inactivation models at a temperature range of 40–70 °C. Kinetic modeling showed that the first-order model and Weibull distribution were the best equations to describe the residual activity of Lipase PS and Palatase, respectively. The results obtained from the kinetic parameters, decimal reduction time (D and tR), and temperature required (z and z’) indicated a higher thermal stability of Lipase PS compared to Palatase. The activation energy values (Ea) also indicated that higher energy was required to denature bacterial (34.8 kJ mol−1) than fungal (23.3 kJ mol−1) lipase. The thermodynamic inactivation parameters, Gibbs free energy (DG#), entropy (DS#), and enthalpy (DH#) were also determined. The results showed a DG# for Palatase (86.0–92.1 kJ mol−1) lower than for Lipase PS (98.6–104.9 kJ mol−1), and a negative entropic and positive enthalpic contribution for both lipases. A comparative molecular dynamics simulation and structural analysis at 40 °C and 70 °C were also performed.

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Section: Resultssupporting

confidence: 87%

Kinetic Modeling, Thermodynamic Approach and Molecular Dynamics Simulation of Thermal Inactivation of Lipases from Burkholderia cepacia and Rhizomucor miehei

Ortega

Sáez

Palacios

et al. 2022

IJMS

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“…Thus, the lower activity found for peh28 relative to those of Joshi et al can be due to the low degree of esterification of polygalacturonic acid or due to the possible enzyme exolytic action on the substrate. The catalytic efficiency of peh28 was 4.87 ml/mg/s, which was higher than those reported by Maisuria et al [ 82 ] at pH 8.5 and 50 °C and Joshi et al [ 80 ] at pH 9.0 and 40 °C for polygalacturonases/pectinases from different sources. These observations indicate the industrial potential of peh28 and also highlight the importance of feedstock characterization for maximum biomass conversion by the tested enzyme.…”

Section: Biochemical Characterization Of Recombinant Cel12b Cel8c Acontrasting

confidence: 56%

“…Table 4 indicates that the K m of peh28 with polygalacturonic acid, 0.87 mg/ml, is similar to those of commercial polygalacturonases [ 25 ]. On the other hand, the V max of peh28 on polygalacturonic acid, 2.01 µmol/ml/min at 40 °C and pH 5.0, is higher than those of Ortega et al [ 79 ], for commercial pectinases at 30 °C and pH 4.2, and lower than that of Joshi et al [ 80 ], for a marine pectinase from Bacillus subtilis at 40 °C and pH 8.0. Such variations in V max might be due to the dissimilar reaction conditions, including enzyme molar concentration; the better comparator would be k cat , if those concentrations were known.…”

Section: Biochemical Characterization Of Recombinant Cel12b Cel8c Amentioning

confidence: 62%

Molecular and biochemical characterization of recombinant cel12B, cel8C, and peh28 overexpressed in Escherichia coli and their potential in biofuel production

Ibrahim

Jones

Taylor

et al. 2017

Biotechnol Biofuels

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BackgroundThe high crystallinity of cellulosic biomass myofibrils as well as the complexity of their intermolecular structure is a significant impediment for biofuel production. Cloning of celB-, celC-encoded cellulases (cel12B and cel8C) and peh-encoded polygalacturonase (peh28) from Pectobacterium carotovorum subsp. carotovorum (Pcc) was carried out in our previous study using Escherichia coli as a host vector. The current study partially characterizes the enzymes’ molecular structures as well as their catalytic performance on different substrates which can be used to improve their potential for lignocellulosic biomass conversion.Resultsβ-Jelly roll topology, (α/α)6 antiparallel helices and right-handed β-helices were the folds identified for cel12B, cel8C, and peh28, respectively, in their corresponding protein model structures. Purifications of 17.4-, 6.2-, and 6.0-fold, compared to crude extract, were achieved for cel12B and cel8C, and peh28, respectively, using specific membrane ultrafiltrations and size-exclusion chromatography. Avicel and carboxymethyl cellulose (CMC) were substrates for cel12B, whereas for cel8C catalytic activity was only shown on CMC. The enzymes displayed significant synergy on CMC but not on Avicel when tested for 3 h at 45 °C. No observed β-glucosidase activities were identified for cel8C and cel12B when tested on p-nitrophenyl-β-d-glucopyranoside. Activity stimulation of 130% was observed when a recombinant β-glucosidase from Pcc was added to cel8C and cel12B as tested for 3 h at 45 °C. Optimum temperature and pH of 45 °C and 5.4, respectively, were identified for all three enzymes using various substrates. Catalytic efficiencies (k cat/K m) were calculated for cel12B and cel8C on CMC as 0.141 and 2.45 ml/mg/s respectively, at 45 °C and pH 5.0 and for peh28 on polygalacturonic acid as 4.87 ml/mg/s, at 40 °C and pH 5.0. Glucose and cellobiose were the end-products identified for cel8C, cel12B, and β-glucosidase acting together on Avicel or CMC, while galacturonic acid and other minor co-products were identified for peh28 action on pectin.ConclusionsThis study provides some insight into which parameters should be optimized when application of cel8C, cel12B, and peh28 to biomass conversion is the goal.

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“…Bacterial strains producing commercial enzymes are always preferred over fungal strains because of ease of fermentation process (for production) and implementation of strain improvement techniques or any modern technique to increase the production yield (Prathyusha & Suneetha, 2011). Moreover, bacterial pectinases with novel properties have the added advantage that enzyme production is achieved in less time as compared to fungal sources (Joshi et al, 2015).…”

Section: Importance Of Bacterial Production Of Pectinasementioning

confidence: 99%

Review on bacterial production of alkaline pectinase with special emphasis on Bacillus species

Kavuthodi¹,

Sebastian²

2018

Biosci. Biotech. Res. Comm

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Pectinases consist of an exclusive group of enzymes which catalyze the degradation of pectic polymers present in the plant cell walls. Today, pectinases are the upcoming industrially important enzyme having major industrial importance and they hold a leading position among the commercially produced industrial enzymes. Microorganisms including yeast, bacteria, actinomycetes and a large number of fi lamentous fungi are commonly recognized as the best natural sources for the production of pectinase enzyme. The chief source of acidic pectinases is fungi but alkaline pectinases are produced from alkalophilic bacteria, primarily Bacillus spp. The alkaline pectinase has developed as important commercial enzymes with far-fl ung applications mainly in textile processing, bio-scouring of cotton fi bers, degumming and retting of fi ber crops, pretreatment of pectic wastewater etc. This review discusses the microbial production of pectinases with special emphasis on bacterial pectinase from Bacillus spp.

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Characterization, Kinetic, and Thermodynamic Studies of Marine Pectinase FromBacillus subtilis

Cited by 17 publications

References 42 publications

Kinetic Modeling, Thermodynamic Approach and Molecular Dynamics Simulation of Thermal Inactivation of Lipases from Burkholderia cepacia and Rhizomucor miehei

Kinetic Modeling, Thermodynamic Approach and Molecular Dynamics Simulation of Thermal Inactivation of Lipases from Burkholderia cepacia and Rhizomucor miehei

Molecular and biochemical characterization of recombinant cel12B, cel8C, and peh28 overexpressed in Escherichia coli and their potential in biofuel production

Review on bacterial production of alkaline pectinase with special emphasis on Bacillus species

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